Structural highlights
Function
AT1A1_PIG This is the catalytic component of the active enzyme, which catalyzes the hydrolysis of ATP coupled with the exchange of sodium and potassium ions across the plasma membrane. This action creates the electrochemical gradient of sodium and potassium ions, providing the energy for active transport of various nutrients.
Publication Abstract from PubMed
The Na+, K+-adenosine triphosphatase (ATPase) maintains the electrochemical gradients of Na+ and K+ across the plasma membrane-a prerequisite for electrical excitability and secondary transport. Hitherto, structural information has been limited to K+-bound or ouabain-blocked forms. We present the crystal structure of a Na+-bound Na+,K+-ATPase as determined at 4.3 A resolution. Compared with the K+-bound form, large conformational changes are observed in the alpha subunit, whereas the beta and gamma subunit structures are maintained. The locations of the three Na+ sites are indicated with the unique site III at the recently suggested IIIb, as further supported by electrophysiological studies on leak currents. Extracellular release of the third Na+ from IIIb through IIIa, followed by exchange of Na+ for K+ at sites I and II, is suggested.
Crystal Structure of Na+, K+-ATPase in the Na+-Bound State.,Nyblom M, Poulsen H, Gourdon P, Reinhard L, Andersson M, Lindahl E, Fedosova N, Nissen P Science. 2013 Sep 19. PMID:24051246[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Nyblom M, Poulsen H, Gourdon P, Reinhard L, Andersson M, Lindahl E, Fedosova N, Nissen P. Crystal Structure of Na+, K+-ATPase in the Na+-Bound State. Science. 2013 Sep 19. PMID:24051246 doi:10.1126/science.1243352
